Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects

Superoxide Dismutase

McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952 · see citing works

Nitric Oxide and Peroxynitrite in Health and Disease

Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works

Hydroperoxide metabolism in mammalian organs.

Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works

A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis

Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, R., Ellis, M. C., Fullan, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0896-399 · Cited by 3,664 · see citing works

Cloning and characterization of a mammalian proton-coupled metal-ion transporter

Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166 · see citing works

The ferritins: molecular properties, iron storage function and cellular regulation

Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667 · see citing works

H ₂ O ₂ , a Necessary Evil for Cell Signaling

Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160 · see citing works

Disorders of Iron Metabolism

Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130 · see citing works

Iron, brain ageing and neurodegenerative disorders

Zecca, L., Youdim, M. B. H., Riederer, P., Connor, J. R., & Crichton, R. R. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1537 · Cited by 1,801 · see citing works

Redefining Oxidative Stress

Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726 · see citing works

Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter

Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667 · see citing works

A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation

McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422 · see citing works

A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism

Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267 · see citing works

Oxygen radicals and signaling

Finkel, T. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80147-6 · Cited by 1,170 · see citing works

Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene

Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159 · see citing works

An iron-regulated ferric reductase associated with the absorption of dietary iron

McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., et al. (2001) · Science · doi:10.1126/science.1057206 · Cited by 1,101 · see citing works

Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse

Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084 · see citing works

Iron metabolism and toxicity

Papanikolaou, G., & Pantopoulos, K. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.06.021 · Cited by 1,070 · see citing works

Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression

Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026 · see citing works

Hereditary Hemochromatosis — A New Look at an Old Disease

Pietrangelo, A. (2004) · New England Journal of Medicine · doi:10.1056/nejmra031573 · Cited by 992 · see citing works

Oxidative Stress: Introductory Remarks

Sies, H. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-642760-8.50005-3 · Cited by 989 · see citing works

Mutations in HFE2 cause iron overload in chromosome 1q–linked juvenile hemochromatosis

Papanikolaou, G., Samuels, M. E., Ludwig, E. H., MacDonald, M. L. E., Franchini, P. L., Dubé, M.-P., Andres, L., MacFarlane, J., Sakellaropoulos, N., Politou, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1274 · Cited by 974 · see citing works

Specific and Reversible Inactivation of Protein Tyrosine Phosphatases by Hydrogen Peroxide: Evidence for a Sulfenic Acid Intermediate and Implications for Redox Regulation

Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945 · see citing works

<i>Nramp</i> <i>2</i> is mutated in the anemic Belgrade ( <i>b</i> ) rat: Evidence of a role for Nramp2 in endosomal iron transport

Fleming, M. D., Romano, M. A., Su, M. A., Garrick, L. M., Garrick, M. D., & Andrews, N. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.1148 · Cited by 936 · see citing works

Biologically relevant metal ion‐dependent hydroxyl radical generation An update

Halliwell, B. B., & Gutteridge, J. M. C. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80911-y · Cited by 884 · see citing works

Calcium and oxidative stress: from cell signaling to cell death

Ermak, G., & Davies, K. J. A. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(01)00108-0 · Cited by 874 · see citing works

Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis

Roetto, A., Papanikolaou, G., Politou, M., Alberti, F., Girelli, D., Christakis, J., Loukopoulos, D., & Camaschella, C. (2003) · Nature Genetics · doi:10.1038/ng1053 · Cited by 860 · see citing works

[5] Diversity of glutathione peroxidases

Maiorino, F. M., Brigelius‐Flohé, R., Aumann, K. D., Roveri, A., Schomburg, D., & Flohé, L. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52007-4 · Cited by 854 · see citing works

Identification of an Intestinal Folate Transporter and the Molecular Basis for Hereditary Folate Malabsorption

Qiu, A., Jansen, M., Sakaris, A., Min, S. H., Chattopadhyay, S., Tsai, E., Sandoval, C., Zhao, R., Akabas, M. H., & Goldman, I. D. (2006) · Cell · doi:10.1016/j.cell.2006.09.041 · Cited by 847 · see citing works

The labile iron pool: characterization, measurement, and participation in cellular processes1 1This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.

Kakhlon, O., & Cabantchik, Z. I. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01006-7 · Cited by 839 · see citing works

Penetrance of 845G→A (C282Y) HFE hereditary haemochromatosis mutation in the USA

Beutler, E., Felitti, V. J., Koziol, J. A., Ho, N. J., & Gelbart, T. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07447-0 · Cited by 823 · see citing works

The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22

Camaschella, C., Roetto, A., Calì, A., De Gobbi, M., Garozzo, G., Carella, M., Majorano, N., Totaro, A., & Gasparini, P. (2000) · Nature Genetics · doi:10.1038/75534 · Cited by 803 · see citing works

Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite, and carbon dioxide

Squadrito, G. L., & Pryor, W. A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00095-1 · Cited by 795 · see citing works

Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells

Ohgami, R. S., Campagna, D. R., Greer, E. L., Antiochos, B., McDonald, A., Chen, J., Sharp, J. J., Fujiwara, Y., Barker, J. E., & Fleming, M. D. (2005) · Nature Genetics · doi:10.1038/ng1658 · Cited by 775 · see citing works

Regulation of Iron Metabolism by Hepcidin

Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756 · see citing works

Identification of an Intestinal Heme Transporter

Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S., Laftah, A. H., Takeuchi, K., Halliday, N., Khan, Y., Warley, A., McCann, F. E., Hider, R. C., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.025 · Cited by 755 · see citing works

The mitochondrial‐lysosomal axis theory of aging

Brunk, U. T., & Terman, A. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02869.x · Cited by 729 · see citing works

The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer

Kalinowski, D. S., & Richardson, D. R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.2 · Cited by 721 · see citing works

Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

Rhee, S. G., Kang, S. W., Jeong, W., Chang, T.-S., Yang, K., & Woo, H. A. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.02.004 · Cited by 709 · see citing works

Ferritin heavy chain upregulation by NF-κB inhibits TNFα-induced apoptosis by suppressing reactive oxygen species

Pham, C. G., Bubici, C., Zazzeroni, F., Papa, S., Jones, J., Alvarez, K., Jayawardena, S., De Smaele, E., Cong, R., Beaumont, C., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.017 · Cited by 663 · see citing works

Iron Homeostasis

Andrews, N. C., & Schmidt, P. J. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.164337 · Cited by 640 · see citing works

Mitoferrin is essential for erythroid iron assimilation

Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624 · see citing works

Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis

Bridle, K. R., Frazer, D. M., Wilkins, S. J., Dixon, J. L., Purdie, D. M., Crawford, D. H., Subramaniam, V. N., Powell, L. W., Anderson, G. J., & Ramm, G. A. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12602-5 · Cited by 620 · see citing works

The transferrin receptor: role in health and disease

Ponka, P., & Lok, C. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00070-9 · Cited by 598 · see citing works

Transferrin receptor is necessary for development of erythrocytes and the nervous system

Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574 · see citing works

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K., Kang, S. W., Kim, K., & Rhee, S. G. (2003) · Science · doi:10.1126/science.1080273 · Cited by 558 · see citing works

Autosomal-dominant hemochrom-atosis is associated with a mutation in the ferroportin (SLC11A3) gene

Montosi, G., Donovan, A., Totaro, A., Garuti, C., Pignatti, E., Cassanelli, S., Trenor, C. C., Gasparini, P., Andrews, N. C., & Pietrangelo, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113468 · Cited by 557 · see citing works

Autosomal-dominant hemochrom-atosis is associated with a mutation in the ferroportin (SLC11A3) gene

Montosi, G., Donovan, A., Totaro, A., Garuti, C., Pignatti, E., Cassanelli, S., Trenor, C. C., Gasparini, P., Andrews, N. C., & Pietrangelo, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13468 · Cited by 555 · see citing works

Tissue-Specific Regulation of Iron Metabolism and Heme Synthesis: Distinct Control Mechanisms in Erythroid Cells

Ponka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544 · see citing works

Redox signaling in macrophages.

Forman, H., & Torres, M. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(01)00010-3 · Cited by 539 · see citing works

HFE gene knockout produces mouse model of hereditary hemochromatosis

Zhou, X. Y., Tomatsu, S., Fleming, R. E., Parkkila, S., Waheed, A., Jiang, J., Fei, Y., Brunt, E. M., Ruddy, D. A., Prass, C. E., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2492 · Cited by 519 · see citing works

A site-specific mechanism for free radical induced biological damage: The essential role of redox-active transition metals

Chevion, M. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90059-7 · Cited by 506 · see citing works

Iron Metabolism and the IRE/IRP Regulatory System: An Update

Pantopoulos, K. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.001 · Cited by 505 · see citing works

A mutation in SLC11A3 is associated with autosomal dominant hemochromatosis

Njajou, O. T., Vaessen, N., Joosse, M., Berghuis, B., van Dongen, J. W. F., Breuning, M. H., Snijders, P. J. L. M., Rutten, W. P. F., Sandkuijl, L. A., Oostra, B. A., et al. (2001) · Nature Genetics · doi:10.1038/90038 · Cited by 492 · see citing works

Hepcidin in iron overload disorders

Papanikolaou, G., Tzilianos, M., Christakis, J. I., Bogdanos, D., Tsimirika, K., MacFarlane, J., Goldberg, Y. P., Sakellaropoulos, N., Ganz, T., & Nemeth, E. (2005) · Blood · doi:10.1182/blood-2004-12-4844 · Cited by 445 · see citing works

Dynamic redox control of NF-κB through glutaredoxin-regulated S-glutathionylation of inhibitory κB kinase β

Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603290103 · Cited by 442 · see citing works

The Broad Spectrum of Responses to Oxidants in Proliferating Cells: A New Paradigm for Oxidative Stress

Davies, K. J. A. (1999) · IUBMB Life · doi:10.1080/713803463 · Cited by 438 · see citing works

Mitochondrial free radical production and cell signaling

Cadenas, E. (2004) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2004.02.005 · Cited by 430 · see citing works

Nramp2 is mutated in the anemic Belgrade (b) rat : evidence of a role for Nramp2 in endosomal iron transport

Flemming (1998) · Medical Entomology and Zoology · Cited by 412 · see citing works

Biosynthesis of nitric oxide activates iron regulatory factor in macrophages.

Drapier, J. C., Hirling, H., Wietzerbin, J., Kaldy, P., & Kühn, L. C. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06038.x · Cited by 401 · see citing works

Hepcidin is decreased in TFR2 hemochromatosis

Nemeth, E., Roetto, A., Garozzo, G., Ganz, T., & Camaschella, C. (2004) · Blood · doi:10.1182/blood-2004-08-3042 · Cited by 396 · see citing works

Fluorescence analysis of the labile iron pool of mammalian cells

Epsztejn, S., Kakhlon, O., Glickstein, H., Breuer, W., & Cabantchik, Z. I. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2126 · Cited by 391 · see citing works

Translational regulation via iron‐responsive elements by the nitric oxide/NO‐synthase pathway.

Weiss, G., Goossen, B., Doppler, W., Fuchs, D., Pantopoulos, K., Werner‐Felmayer, G., Wachter, H., & Hentze, M. W. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06039.x · Cited by 389 · see citing works

Molecular bases of cellular iron toxicity12 1Guest Editor: Mario Comporti 2This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.

Eaton, J. W., & Qian, M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00772-4 · Cited by 389 · see citing works

The ferroportin disease

Pietrangelo, A. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2003.08.003 · Cited by 380 · see citing works

Controlled Elimination of Intracellular H ₂ O2: Regulation of Peroxiredoxin, Catalase, and Glutathione Peroxidase via Post-translational Modification

Rhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376 · see citing works

Heme oxygenase and the cardiovascular–renal system

Abraham, N. G., & Kappas, A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.010 · Cited by 356 · see citing works

Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing.

Goswami, T., & Andrews, N. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600197200 · Cited by 352 · see citing works

The role of cysteine residues as redox-sensitive regulatory switches

Barford, D. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.09.012 · Cited by 331 · see citing works

Rapid responses to oxidative stress mediated by iron regulatory protein.

Pantopoulos, K., & Hentze, M. W. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07291.x · Cited by 328 · see citing works

Coordinated Regulation of Iron-Controlling Genes, H-Ferritin and IRP2 , by c-MYC

Wu, K., Polack, A., & Dalla‐Favera, R. (1999) · Science · doi:10.1126/science.283.5402.676 · Cited by 328 · see citing works

Transient Adaptation to Oxidative Stress in Mammalian Cells

Wiese, A. G., Pacifici, R. E., & Davies, K. J. A. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1225 · Cited by 298 · see citing works

Design of iron chelators with therapeutic application

Liu, Z. D., & Hider, R. C. (2002) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(02)00050-4 · Cited by 287 · see citing works

Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture

Antunes, F., Cadenas, E., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560549 · Cited by 286 · see citing works

Design of clinically useful iron(III)‐selective chelators

Liu, Z. D., & Hider, R. C. (2002) · Medicinal Research Reviews · doi:10.1002/med.1027 · Cited by 266 · see citing works

The C282Y Mutation Causing Hereditary Hemochromatosis Does Not Produce a Null Allele

Levy, J. E., Montross, L. K., Cohen, D. E., Fleming, M. D., & Andrews, N. C. (1999) · Blood · doi:10.1182/blood.v94.1.9.413a43_9_11 · Cited by 259 · see citing works

Heme Oxygenase-1: Redox Regulation of a Stress Protein in Lung and Cell Culture Models

Ryter, S. W., & Choi, A. M. K. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.80 · Cited by 244 · see citing works

Overexpression of Wild Type and Mutated Human Ferritin H-chain in HeLa Cells

Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Albertini, A., & Arosio, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003797200 · Cited by 242 · see citing works

Juvenile Hemochromatosis Locus Maps to Chromosome 1q

Roetto, A., Totaro, A., Cazzola, M., Cicilano, M., Bosio, S., D’Ascola, D. G., Carella, M., Zelante, L., Kelly, A., Cox, T. M., et al. (1999) · The American Journal of Human Genetics · doi:10.1086/302379 · Cited by 235 · see citing works

Ferroportin‐mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome

De Domenico, I., Vaughn, M. B., Li, L., Bagley, D., Musci, G., Ward, D. M., & Kaplan, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601409 · Cited by 235 · see citing works

Iron, Free Radicals, and Oxidative Injury

McCord, J. M. (2004) · Journal of Nutrition · doi:10.1093/jn/134.11.3171s · Cited by 232 · see citing works

Intralysosomal iron: a major determinant of oxidant-induced cell death

Yu, Z., Persson, H. L., Eaton, J. W., & Brunk, U. T. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00109-6 · Cited by 226 · see citing works

Free radical biology – terminology and critical thinking

Azzi, A., Davies, K. J. A., & Kelly, F. J. (2004) · FEBS Letters · doi:10.1016/s0014-5793(03)01526-6 · Cited by 205 · see citing works

Iron Chelators in Cancer Chemotherapy

Buss, J. L., Greene, B. T., Turner, J., Torti, F. M., & Torti, S. V. (2004) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026043387269 · Cited by 199 · see citing works

Nitric Oxide and Oxidative Stress (H₂O₂) Control Mammalian Iron Metabolism by Different Pathways

Pantopoulos, K., Weiss, G., & Hentze, M. W. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3781 · Cited by 195 · see citing works

Understanding iron homeostasis through genetic analysis of hemochromatosis and related disorders

Camaschella, C. (2005) · Blood · doi:10.1182/blood-2005-05-1857 · Cited by 194 · see citing works

Intracellular iron, but not copper, plays a critical role in hydrogen peroxide-induced DNA Damage

Barbouti, A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00608-6 · Cited by 190 · see citing works

Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice

Gunshin, H., Starr, C. N., DiRenzo, C., Fleming, M. D., Jin, J., Greer, E. L., Sellers, V. M., Galica, S. M., & Andrews, N. C. (2005) · Blood · doi:10.1182/blood-2005-02-0716 · Cited by 188 · see citing works

Prevention of oxidant-induced cell death by lysosomotropic iron chelators

Persson, H. L., Yu, Z., Tirosh, O., Eaton, J. W., & Brunk, U. T. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00106-0 · Cited by 185 · see citing works

Use and abuse of exogenous H2O2 in studies of signal transduction

Forman, H. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.011 · Cited by 182 · see citing works

Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture

Antunes, F., Cadenas, E., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/bj3560549 · Cited by 181 · see citing works

Ferritins: iron/oxygen biominerals in protein nanocages

Theil, E. C., Matzapetákis, M., & Liu, X. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0125-6 · Cited by 175 · see citing works

Mechanisms of iron–sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes

Lill, R., Dutkiewicz, R., Elsässer, H., Hausmann, A., Netz, D. J. A., Pierik, A. J., Stehling, O., Urzica, E. I., & Mühlenhoff, U. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.011 · Cited by 170 · see citing works

Differences in the Regulation of Iron Regulatory Protein-1 (IRP-1) by Extra- and Intracellular Oxidative Stress

Pantopoulos, K., Mueller, S., Atzberger, A., Ansorge, W. J., Stremmel, W., & Hentze, M. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.9802 · Cited by 163 · see citing works

Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts

Radisky, D. C., & Kaplan, J. (1998) · Biochemical Journal · doi:10.1042/bj3360201 · Cited by 163 · see citing works

Signaling Role of Intracellular Iron in NF-κB Activation

Xiong, S., She, H., Takeuchi, H., Han, B., Engelhardt, J. F., Barton, C. H., Zandi, E., Giulivi, C., & Tsukamoto, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210905200 · Cited by 161 · see citing works

Sites and Mechanisms of Aconitase Inactivation by Peroxynitrite:  Modulation by Citrate and Glutathione

Han, D., Canali, R., Garcia, J., Aguilera, R., Gallaher, T. K., & Cadenas, E. (2005) · Biochemistry · doi:10.1021/bi0509393 · Cited by 161 · see citing works

Ca2+ channel blockers reverse iron overload by a new mechanism via divalent metal transporter-1

Ludwiczek, S., Theurl, I., Muckenthaler, M. U., Jakab, M., Mair, S. M., Theurl, M., Kiss, J., Paulmichl, M., Hentze, M. W., Ritter, M., et al. (2007) · Nature Medicine · doi:10.1038/nm1542 · Cited by 160 · see citing works

Iron is the intracellular metal involved in the production of DNA damage by oxygen radicals

Mello-Filho, A. C., & Meneghini, R. (1991) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/0027-5107(91)90220-i · Cited by 159 · see citing works

Unexpected role of ceruloplasmin in intestinal iron absorption

Cherukuri, S., Potla, R., Sarkar, J., Nurko, S., Harris, Z. L., & Fox, P. L. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.003 · Cited by 158 · see citing works

Oxidative Stress Induces Activation of a Cytosolic Protein Responsible for Control of Iron Uptake

Martins, E. A. L., Robalinho, R. L., & Meneghini, R. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1019 · Cited by 148 · see citing works

Does the calcein-AM method assay the total cellular ‘labile iron pool’ or only a fraction of it?

Τενοπούλου, Μ., Kurz, T., Doulias, P., Galaris, D., & Brunk, U. T. (2007) · Biochemical Journal · doi:10.1042/bj20061840 · Cited by 146 · see citing works

Metallothionein protects against oxidative stress-induced lysosomal destabilization

Baird, S. K., Kurz, T., & Brunk, U. T. (2006) · Biochemical Journal · doi:10.1042/bj20051143 · Cited by 145 · see citing works

Localized Unfolding at the Junction of Three Ferritin Subunits

Takagi, H., Shi, D., Ha, Y., Allewell, N. M., & Theil, E. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18685 · Cited by 130 · see citing works

Iron activates NF-κB in Kupffer cells

She, H., Xiong, S., Lin, M., Zandi, E., Giulivi, C., & Tsukamoto, H. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00108.2002 · Cited by 121 · see citing works

Potent Antitumor Activity of Novel Iron Chelators Derived from Di-2-Pyridylketone Isonicotinoyl Hydrazone Involves Fenton-Derived Free Radical Generation

Chaston, T. B., Watts, R., Yuan, J. J., & Richardson, D. R. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-0865 · Cited by 120 · see citing works

Mitochondrial ferritin

Levi, S., & Arosio, P. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.10.020 · Cited by 120 · see citing works

Involvement of JNKs and p38-MAPK/MSK1 pathways in H2O2-induced upregulation of heme oxygenase-1 mRNA in H9c2 cells

Aggeli, I.-K. S., Gaitanaki, C., & Beis, I. D. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.02.001 · Cited by 119 · see citing works

Modulation of Cellular Iron Metabolism by Hydrogen Peroxide

Caltagirone, A., Weiß, G., & Pantopoulos, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100245200 · Cited by 118 · see citing works

Iron Chelator Research: Past, Present, and Future

Tam, T. F., Leung-Toung, R., Li, W., Wang, Y., Karimian, K., & Spino, M. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033457593 · Cited by 117 · see citing works

Desferoxamine (DFO)—Mediated iron chelation: Rationale for a novel approach to therapy for brain cancer

Dayani, P. N., Bishop, M. C., Black, K., & Zeltzer, P. M. (2004) · Journal of Neuro-Oncology · doi:10.1023/b:neon.0000024238.21349.37 · Cited by 114 · see citing works

Determination of the Chelatable Iron Pool of Single Intact Cells by Laser Scanning Microscopy

Petrat, F., de GROOT, H., & Rauen, U. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1711 · Cited by 112 · see citing works

Redox cycling of myoglobin and ascorbate: A potential protective mechanism against oxidative reperfusion injury in muscle

Galaris, D., Cadenas, E., & Hochstein, P. E. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90509-2 · Cited by 110 · see citing works

Role of compartmentalized redox-active iron in hydrogen peroxide-induced DNA damage and apoptosis

Τενοπούλου, Μ., Doulias, P., Barbouti, A., Brunk, U. T., & Galaris, D. (2005) · Biochemical Journal · doi:10.1042/bj20041650 · Cited by 109 · see citing works

Myeloperoxidase-derived Hypochlorous Acid Antagonizes the Oxidative Stress-mediated Activation of Iron Regulatory Protein 1

Mütze, S., Hebling, U., Stremmel, W., Wang, J., Arnhold, J., Pantopoulos, K., & Mueller, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307159200 · Cited by 101 · see citing works

Hereditary Causes of Disturbed Iron Homeostasis in the Central Nervous System

Ponka, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.022 · Cited by 99 · see citing works

Iron Chelators as Anti-Neoplastic Agents: Current Developments and Promise of the PIH Class of Chelators

Lovejoy, D., & Richardson, D. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033457557 · Cited by 98 · see citing works

Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells

Kakhlon, O., Gruenbaum, Y., & Cabantchik, Z. I. (2001) · Blood · doi:10.1182/blood.v97.9.2863 · Cited by 97 · see citing works

Endosomal and lysosomal effects of desferrioxamine: protection of HeLa cells from hydrogen peroxide-induced DNA damage and induction of cell-cycle arrest

Doulias, P., Christoforidis, S., Brunk, U. T., & Galaris, D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00396-4 · Cited by 96 · see citing works

Oxidative Stress in Hepatic Ischemia-Reperfusion Injury: The Role of Antioxidants and Iron Chelating Compounds

Galaris, D., Barbouti, A., & Korantzopoulos, P. G. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206777947614 · Cited by 96 · see citing works

Fenton Chemistry and Iron Chelation under Physiologically Relevant Conditions: Electrochemistry and Kinetics

Merkofer, M., Kissner, R., Hider, R. C., Brunk, U. T., & Koppenol, W. H. (2006) · Chemical Research in Toxicology · doi:10.1021/tx060101w · Cited by 95 · see citing works

Mechanisms of reoxygenation injury in myocardial infarction: Implications of a myoglobin redox cycle

Galaris, D., Eddy, L. J., Arduini, A., Cadenas, E., & Hochstein, P. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(89)80125-1 · Cited by 95 · see citing works

Oxidation-induced ferritin turnover in microglial cells: role of proteasome

Mehlhase, J., Sandig, G., Pantopoulos, K., & Grune, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.025 · Cited by 84 · see citing works

Is stored iron safe?

Sullivan, J. L. (2004) · Journal of Laboratory and Clinical Medicine · doi:10.1016/j.lab.2004.10.006 · Cited by 82 · see citing works

Intracellular metal ion chelators inhibit TNFα-induced SP-1 activation and adhesion molecule expression in human aortic endothelial cells

Zhang, W. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01375-8 · Cited by 70 · see citing works

Juvenile hemochromatosis

Camaschella, C., Roetto, A., & Gobbi, M. D. (2002) · Seminars in Hematology · doi:10.1053/shem.2002.35635 · Cited by 70 · see citing works

The Iron Chelator L1 Potentiates Oxidative DNA Damage in Iron-Loaded Liver Cells

Cragg, L., Hebbel, R. P., Miller, W. J., Solovey, A., Selby, S. A., & Enright, H. (1998) · Blood · doi:10.1182/blood.v92.2.632 · Cited by 66 · see citing works

Intracellular Labile Iron Modulates Adhesion of Human Monocytes to Human Endothelial Cells

Kartikasari, A. E. R., Georgiou, N., Visseren, F. L. J., Kats-Renaud, H. J. V., van Asbeck, B. S., & Marx, J. J. M. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000147406.00871.b3 · Cited by 66 · see citing works

Involvement of heat shock protein-70 in the mechanism of hydrogen peroxide-induced DNA damage: The role of lysosomes and iron

Doulias, P., Kotoglou, P., Τενοπούλου, Μ., Keramisanou, D., Tzavaras, T., Brunk, U. T., Galaris, D., & Angelidis, C. E. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.022 · Cited by 65 · see citing works

Iron Causes Interactions of TAK1, p21ras, and Phosphatidylinositol 3-Kinase in Caveolae to Activate IκB Kinase in Hepatic Macrophages

Chen, L., Xiong, S., She, H., Lin, S. W., Wang, J., & Tsukamoto, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609273200 · Cited by 64 · see citing works

Serum markers of stored body iron are not appropriate markers of health effects of iron: a focus on serum ferritin

Lee, D.-H., & Jacobs, D. R. (2004) · Medical Hypotheses · doi:10.1016/s0306-9877(03)00344-x · Cited by 54 · see citing works

Iron Chelation Inhibits NF-κB–Mediated Adhesion Molecule Expression by Inhibiting p22 ^phox Protein Expression and NADPH Oxidase Activity

Li, L., & Frei, B. (2006) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000245820.34238.da · Cited by 49 · see citing works

On the Molecular Mechanism of Metmyoglobin-Catalyzed Reduction of Hydrogen Peroxide by Ascorbate

Galaris, D., & Korantzopoulos, P. G. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00382-6 · Cited by 42 · see citing works

Nitric Oxide Inhibits the Degradation of IRP2

Wang, J., Chen, G., & Pantopoulos, K. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1347-1353.2005 · Cited by 38 · see citing works

β-Thalassaemia: emergence of new and improved iron chelators for treatment

Wong, C. S., & Richardson, D. R. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00046-3 · Cited by 36 · see citing works

Linkage to Chromosome 1q in Greek Families with Juvenile Hemochromatosis

Papanikolaou, G. V., Politou, M., Roetto, A., Bosio, S., Sakelaropoulos, N., Camaschella, C., & Λουκόπουλος, Δ. (2001) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2001.0444 · Cited by 33 · see citing works

Cross-compartment protection by SOD1

Liochev, S. I., & Fridovich, I. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.017 · Cited by 32 · see citing works

When Is a Heme Transporter Not a Heme Transporter? When It's a Folate Transporter

Andrews, N. C. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.12.004 · Cited by 31 · see citing works

New developments in iron chelators

Cunningham, M. J., & Nathan, D. G. (2005) · Current Opinion in Hematology · doi:10.1097/01.moh.0000152631.63469.07 · Cited by 31 · see citing works

Juvenile hemochromatosis locus maps to chromosome 1q in a French Canadian population

Rivard, S. R., Lanzara, C., Grimard, D., Carella, M., Simard, H., Ficarella, R., Simard, R., D’Adamo, P., Férec, C., Camaschella, C., et al. (2003) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201009 · Cited by 29 · see citing works

NF-κB meets ROS: an ‘iron-ic’ encounter

Papa, S., Bubici, C., Pham, C. G., Zazzeroni, F., & Franzoso, G. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401694 · Cited by 24 · see citing works

Desferrithiocin Analogue Based Hexacoordinate Iron(III) Chelators

Bergeron, R. J., Huang, G., Weimar, W. R., Smith, R. E., Wiegand, J., & McManis, J. S. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm020184n · Cited by 22 · see citing works

Iron-binding drugs targeted to lysosomes: a potential strategy to treat inflammatory lung disorders

Persson, H. L., & Richardson, D. R. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.8.997 · Cited by 21 · see citing works

Hemochromatosis

Adams, P. C. (2004) · Clinics in Liver Disease · doi:10.1016/j.cld.2004.06.002 · Cited by 20 · see citing works

Juvenile hemochromatosis

Pietrangelo, A. (2006) · Journal of Hepatology · doi:10.1016/j.jhep.2006.09.003 · Cited by 18 · see citing works

Genetic Heterogeneity Underlies Juvenile Hemochromatosis Phenotype: Analysis of Three Families of Northern Greek Origin

Papanikolaou, G. V., Papaioannou, M., Politou, M., Vavatsi, N. A., Kioumi, A., Τσιάτσιου, Π., Marinaki, P., Loukopoulos, D., & Christakis, J. I. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0553 · Cited by 17 · see citing works

Regulation of cellular iron metabolism

Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986 · see citing works

Triggering and resolution of inflammation in NASH

Schuster, S., Cabrera, D., Arrese, M., & Feldstein, A. E. (2018) · Nature Reviews Gastroenterology &amp; Hepatology · doi:10.1038/s41575-018-0009-6 · Cited by 943 · see citing works

Iron homeostasis and oxidative stress: An intimate relationship

Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 922 · see citing works

Common Genetic Variation In Cellular Transport Genes and Epithelial Ovarian Cancer (EOC) Risk

Chornokur, G., Lin, H., Tyrer, J. P., Lawrenson, K., Dennis, J., Amankwah, E. K., Qu, X., Tsai, Y.-Y., Jim, H., Chen, Z., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128106 · Cited by 907 · see citing works

Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases

Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works

Metals, oxidative stress and neurodegeneration: A focus on iron, manganese and mercury

Farina, M., Ávila, D. S., da Rocha, J. B. T., & Aschner, M. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.12.006 · Cited by 558 · see citing works

Regulation of the Iron Homeostatic Hormone Hepcidin

Sangkhae, V., & Nemeth, E. (2017) · Advances in Nutrition · doi:10.3945/an.116.013961 · Cited by 446 · see citing works

Bone loss caused by iron overload in a murine model: importance of oxidative stress.

Tsay, J., Yang, Z., Ross, F., Cunningham-Rundles, S., Lin, H., Coleman, R. M., Mayer-Kuckuk, P., Doty, S. B., Grady, R., Giardina, P., et al. (2010) · Blood · doi:10.1182/blood-2009-12-260083 · Cited by 336 · see citing works

Minerals and Sarcopenia; The Role of Calcium, Iron, Magnesium, Phosphorus, Potassium, Selenium, Sodium, and Zinc on Muscle Mass, Muscle Strength, and Physical Performance in Older Adults: A Systematic Review

van Dronkelaar, C., van Velzen, A., Abdelrazek, M., van der Steen, A., Weijs, P. J. M., & Tieland, M. (2018) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2017.05.026 · Cited by 279 · see citing works

Altered Iron Metabolism and Impact in Cancer Biology, Metastasis, and Immunology

Brown, R. A. M., Richardson, K. L., Kabir, T. D., Trinder, D., Ganß, R., & Leedman, P. J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00476 · Cited by 279 · see citing works

Free radical biology for medicine: learning from nonalcoholic fatty liver disease

Serviddio, G., Bellanti, F., & Vendemiale, G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.174 · Cited by 269 · see citing works

Synthetic and natural iron chelators: Therapeutic potential and clinical use

Hatcher, H. C., Singh, R. N., Torti, F. M., & Torti, S. V. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.121 · Cited by 242 · see citing works

Iron deficiency and cardiovascular disease

Savarese, G., von Haehling, S., Butler, J., Cleland, J. G. F., Ponikowski, P. P., & Anker, S. D. (2022) · European Heart Journal · doi:10.1093/eurheartj/ehac569 · Cited by 203 · see citing works

Iron and Chelation in Biochemistry and Medicine: New Approaches to Controlling Iron Metabolism and Treating Related Diseases

Kontoghiorghes, G. J., & Kontoghiorghe, C. (2020) · Cells · doi:10.3390/cells9061456 · Cited by 197 · see citing works

Resveratrol Protects Mitochondria against Oxidative Stress through AMP-Activated Protein Kinase-Mediated Glycogen Synthase Kinase-3β Inhibition Downstream of Poly(ADP-ribose)polymerase-LKB1 Pathway

Shin, S. M., Cho, I. J., & Kim, S. G. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.058479 · Cited by 195 · see citing works

Iron Accumulates in Huntington’s Disease Neurons: Protection by Deferoxamine

Chen, J., Marks, E. S., Lai, B. C. H., Zhang, Z., Duce, J. A., Lam, L. Q., Volitakis, I., Bush, A. I., Hersch, S. M., & Fox, J. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077023 · Cited by 176 · see citing works

The role of antioxidant supplement in immune system, neoplastic, and neurodegenerative disorders: a point of view for an assessment of the risk/benefit profile

Brambilla, D., Mancuso, C., Scuderi, M. G., Bosco, P., Cantarella, G., Lempereur, L., Benedetto, G. D., Pezzino, S., & Bernardini, R. (2008) · Nutrition Journal · doi:10.1186/1475-2891-7-29 · Cited by 153 · see citing works

Isoquercitrin is the most effective antioxidant in the plant Thuja orientalis and able to counteract oxidative-induced damage to a transformed cell line (RGC-5 cells)

Jung, S. H., Kim, B. J., Lee, E. H., & Osborne, N. N. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.08.005 · Cited by 144 · see citing works

General Trends in Trace Element Utilization Revealed by Comparative Genomic Analyses of Co, Cu, Mo, Ni, and Se

Zhang, Y., & Gladyshev, V. N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071746 · Cited by 142 · see citing works

Ferroptosis in sepsis: The mechanism, the role and the therapeutic potential

Lei, X. L., Zhao, G. Y., Guo, R., & Cui, N. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.956361 · Cited by 152 · see citing works

Diagnostic morphology: biophysical indicators for iron-driven inflammatory diseases

Pretorius, E., & Kell, D. B. (2014) · Integrative Biology · doi:10.1039/c4ib00025k · Cited by 141 · see citing works

Ferroptosis Signaling and Regulators in Atherosclerosis

Wang, Y., Zhao, Y., Ye, T., Yang, L. M., Shen, Y., & Li, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.809457 · Cited by 135 · see citing works

Comparative Genomics of Trace Elements: Emerging Dynamic View of Trace Element Utilization and Function

Zhang, Y., & Gladyshev, V. N. (2009) · Chemical Reviews · doi:10.1021/cr800557s · Cited by 143 · see citing works

Cell Death Pathways: a Novel Therapeutic Approach for Neuroscientists

Morris, G., Walker, A. J., Berk, M., Maes, M. H. J., & Puri, B. K. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0793-y · Cited by 129 · see citing works

Iron deficiency beyond erythropoiesis: should we be concerned?

Musallam, K. M., & Taher, A. T. (2017) · Current Medical Research and Opinion · doi:10.1080/03007995.2017.1394833 · Cited by 122 · see citing works

Facilitated Diffusion of Iron(II) and Dioxygen Substrates into Human H-Chain Ferritin. A Fluorescence and Absorbance Study Employing the Ferroxidase Center Substitution Y34W

Bou‐Abdallah, F., Zhao, G., Biasiotto, G., Poli, M., Arosio, P., & Chasteen, N. D. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8054035 · Cited by 122 · see citing works

AMPK-mediated GSK3β inhibition by isoliquiritigenin contributes to protecting mitochondria against iron-catalyzed oxidative stress

Choi, S. H., Kim, Y. W., & Kim, S. G. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.12.011 · Cited by 115 · see citing works

Ferroptosis: Final destination for cancer?

Zeng, Y., Liu, W., Zhuo, Q., Hu, Q., Liu, M., Sun, Q., Zhang, Z., Fan, G., Xu, W., Ji, S., et al. (2020) · Cell Proliferation · doi:10.1111/cpr.12761 · Cited by 115 · see citing works

Iron intake, body iron status, and risk of breast cancer: a systematic review and meta-analysis

Chang, V. C., Cotterchio, M., & Khoo, E. (2019) · BMC Cancer · doi:10.1186/s12885-019-5642-0 · Cited by 111 · see citing works

Trying to Solve the Puzzle of the Interaction of Ascorbic Acid and Iron: Redox, Chelation and Therapeutic Implications

Kontoghiorghes, G. J., Kolnagou, A., Kontoghiorghe, C., Mourouzidis, L., Timoshnikov, V. A., & Polyakov, N. E. (2020) · Medicines · doi:10.3390/medicines7080045 · Cited by 110 · see citing works

Efficacy of sauchinone as a novel AMPK-activating lignan for preventing iron-induced oxidative stress and liver injury

Kim, Y. W., Lee, S. M., Shin, S. M., Hwang, S. J., Brooks, J. S., Kang, H. E., Lee, M. G., Kim, S. C., & Kim, S. G. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.018 · Cited by 106 · see citing works

The Dark Side of Iron: The Relationship between Iron, Inflammation and Gut Microbiota in Selected Diseases Associated with Iron Deficiency Anaemia—A Narrative Review

Malesza, I. J., Bartkowiak-Wieczorek, J., Winkler-Galicki, J., Nowicka, A., Dzięciołowska, D., Błaszczyk, M., Gajniak, P., Słowińska, K., Niepolski, L., Walkowiak, J., et al. (2022) · Nutrients · doi:10.3390/nu14173478 · Cited by 109 · see citing works

Regulation of iron pathways in response to hypoxia

Chepelev, N. L., & Willmore, W. G. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.023 · Cited by 102 · see citing works

Use of Superparamagnetic Iron Oxide Nanoparticles (SPIONs) via Multiple Imaging Modalities and Modifications to Reduce Cytotoxicity: An Educational Review

Nelson, N., Port, J. D., & Pandey, M. K. (2020) · Journal of Nanotheranostics · doi:10.3390/jnt1010008 · Cited by 102 · see citing works

Bone Disease in Thalassemia: A Molecular and Clinical Overview

Wong, P., Fuller, P. J., Gillespie, M. T., & Milat, F. (2016) · Endocrine Reviews · doi:10.1210/er.2015-1105 · Cited by 99 · see citing works

Iron overload inhibits late stage autophagic flux leading to insulin resistance

Jahng, J. W. S., Alsaadi, R. M., Palanivel, R., Song, E., Hipolito, V. E. B., Sung, H. K., Botelho, R. J., Russell, R. C., & Sweeney, G. (2019) · EMBO Reports · doi:10.15252/embr.201947911 · Cited by 95 · see citing works

Oxidative Stress-Induced Cellular Senescence: Is Labile Iron the Connecting Link?

Nousis, L., Kanavaros, P., & Barbouti, A. (2023) · Antioxidants · doi:10.3390/antiox12061250 · Cited by 96 · see citing works

Mechanistic Insights of Chelator Complexes with Essential Transition Metals: Antioxidant/Pro-Oxidant Activity and Applications in Medicine

Timoshnikov, V. A., Selyutina, O. Y., Polyakov, N. E., Didichenko, V., & Kontoghiorghes, G. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031247 · Cited by 97 · see citing works

Potential Toxicity and Underlying Mechanisms Associated with Pulmonary Exposure to Iron Oxide Nanoparticles: Conflicting Literature and Unclear Risk

Kornberg, T. G., Stueckle, T. A., Antonini, J. A., Rojanasakul, Y., Castranova, V., Yang, Y. S., & Wang, L. (2017) · Nanomaterials · doi:10.3390/nano7100307 · Cited by 91 · see citing works

Association between dietary nutrient intake and sarcopenia in the SarcoPhAge study

Beaudart, C., Locquet, M., Touvier, M., Reginster, J., & Bruyère, O. (2019) · Aging Clinical and Experimental Research · doi:10.1007/s40520-019-01186-7 · Cited by 89 · see citing works

Neurodegenerative changes and neuroapoptosis induced by systemic lipopolysaccharide administration are reversed by dexmedetomidine treatment in mice

Ning, Q., Liu, Z., Wang, X., Zhang, R., Zhang, J., Yang, M., Sun, H., Han, F., Zhao, W., & Zhang, X. (2017) · Neurological Research · doi:10.1080/01616412.2017.1281197 · Cited by 88 · see citing works

AMPK activation by isorhamnetin protects hepatocytes against oxidative stress and mitochondrial dysfunction

Dong, G.-Z., Lee, J., Ki, S. H., Yang, J. H., Cho, I. J., Kang, S. H., Zhao, R., Kim, S. C., & Kim, Y. W. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.06.017 · Cited by 88 · see citing works

Poorly controlled type 2 diabetes is accompanied by significant morphological and ultrastructural changes in both erythrocytes and in thrombin-generated fibrin: implications for diagnostics

Pretorius, E., Bester, J., Vermeulen, N., Alummoottil, S., Soma, P., Buys, A. V., & Kell, D. B. (2015) · Cardiovascular Diabetology · doi:10.1186/s12933-015-0192-5 · Cited by 87 · see citing works

The effect of exercise on intraocular pressure. I. Human beings.

Marcus, D. F., Krupin, T., Podos, S. M., & BECKER, B. A. (1970) · PubMed · Cited by 84 · see citing works

Implications of Oxidative Stress and Cellular Senescence in Age-Related Thymus Involution

Barbouti, A., Vasileiou, P. V. S., Evangelou, K., Vlasis, K. G., Papoudou‐Bai, A., Gorgoulis, V. G., & Kanavaros, P. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7986071 · Cited by 83 · see citing works

Novel insights into redox system and the mechanism of redox regulation

Wang, X., & Hai, C. (2016) · Molecular Biology Reports · doi:10.1007/s11033-016-4022-y · Cited by 82 · see citing works

Iron Load Toxicity in Medicine: From Molecular and Cellular Aspects to Clinical Implications

Kontoghiorghes, G. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612928 · Cited by 79 · see citing works

Treatment with iron oxide nanoparticles induces ferritin synthesis but not oxidative stress in oligodendroglial cells

Hohnholt, M. C., Geppert, M., & Dringen, R. (2011) · Acta Biomaterialia · doi:10.1016/j.actbio.2011.06.052 · Cited by 73 · see citing works

Discovering the role of mitochondria in the iron deficiency-induced metabolic responses of plants

Vigani, G. (2011) · Journal of Plant Physiology · doi:10.1016/j.jplph.2011.09.008 · Cited by 73 · see citing works

Iron homeostasis and health: understanding its role beyond blood health – a narrative review

Obeagu, E. I. (2025) · Annals of Medicine and Surgery · doi:10.1097/ms9.0000000000003100 · Cited by 84 · see citing works

Hydroxytyrosol inhibits hydrogen peroxide-induced apoptotic signaling via labile iron chelation

Kitsati, N., Mantzaris, M. D., & Galaris, D. (2016) · Redox Biology · doi:10.1016/j.redox.2016.10.006 · Cited by 70 · see citing works

Mitochondrial Iron Metabolism: The Crucial Actors in Diseases

Duan, G., Li, J., Duan, Y., Zheng, C., Guo, Q., Li, F., Zheng, J., Yu, J., Zhang, P., Wan, M., et al. (2022) · Molecules · doi:10.3390/molecules28010029 · Cited by 73 · see citing works

Phytochelators Intended for Clinical Use in Iron Overload, Other Diseases of Iron Imbalance and Free Radical Pathology

Kontoghiorghe, C., Kolnagou, A., & Kontoghiorghes, G. J. (2015) · Molecules · doi:10.3390/molecules201119725 · Cited by 69 · see citing works

Nrf2 regulates iron-dependent hippocampal synapses and functional connectivity damage in depression

Zeng, T., Li, J., Xie, L., Dong, Z., Chen, Q., Huang, S., Xie, S., Lai, Y., Li, J., Yan, W., et al. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02875-x · Cited by 71 · see citing works

Ferrostatin-1 Ameliorates Liver Dysfunction via Reducing Iron in Thioacetamide-induced Acute Liver Injury in Mice

Jiang, H., Zhang, X., Yang, W.-P., Li, M., Wang, G., & Luo, Q. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.869794 · Cited by 67 · see citing works

Dietary Micronutrient and Mineral Intake in the Mediterranean Healthy Eating, Ageing, and Lifestyle (MEAL) Study

Castiglione, D., Platania, A., Conti, A., Falla, M., D’Urso, M., & Marranzano, M. (2018) · Antioxidants · doi:10.3390/antiox7070079 · Cited by 67 · see citing works

The Potential for Transition Metal-Mediated Neurodegeneration in Amyotrophic Lateral Sclerosis

Lovejoy, D. B., & Guillemin, G. J. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00173 · Cited by 65 · see citing works

Unsuspected control of siderophore production by N ‐acetylglucosamine in streptomycetes

Craig, M., Lambert, S., Jourdan, S., Tenconi, E., Colson, S., Maciejewska, M., Ongena, M., Martin, J. F., van Wezel, G. P., & Rigali, S. (2012) · Environmental Microbiology Reports · doi:10.1111/j.1758-2229.2012.00354.x · Cited by 64 · see citing works

Molecular basis of iron-loading disorders

Darshan, D., Frazer, D. M., & Anderson, G. J. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399410001687 · Cited by 63 · see citing works

A novel method for assessing the role of iron and its functional chelation in fibrin fibril formation: the use of scanning electron microscopy

Pretorius, E., Vermeulen, N., Bester, J., Lipiński, B., & Kell, D. B. (2013) · Toxicology Mechanisms and Methods · doi:10.3109/15376516.2012.762082 · Cited by 60 · see citing works

Intracellular labile iron determines H2O2-induced apoptotic signaling via sustained activation of ASK1/JNK-p38 axis

Mantzaris, M. D., Bellou, S., Skiada, V., Kitsati, N., Fotsis, T., & Galaris, D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.07.002 · Cited by 61 · see citing works

Patient-specific hepatocyte-like cells derived from induced pluripotent stem cells model pazopanib-mediated hepatotoxicity

Choudhury, Y., Toh, Y., Xing, J., Qu, Y., Poh, J., Li, H., Tan, H. S., Kanesvaran, R., Yu, H., & Tan, M. (2017) · Scientific Reports · doi:10.1038/srep41238 · Cited by 61 · see citing works

Iron excess limits HHIPL-2 gene expression and decreases osteoblastic activity in human MG-63 cells

Doyard, M., Fatih, N., Monnier, A., Island, M., Aubry, M., Leroyer, P., Bouvet, R., Chalès, G., Mosser, J., Loréal, O., et al. (2012) · Osteoporosis International · doi:10.1007/s00198-011-1871-z · Cited by 58 · see citing works

Red ginseng abrogates oxidative stress via mitochondria protection mediated by LKB1-AMPK pathway

Dong, G.-Z., Jang, E. J., Kang, S. H., Cho, I. J., Park, S., Kim, S. C., & Kim, Y. W. (2013) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-13-64 · Cited by 58 · see citing works

Disorders associated with systemic or local iron overload: from pathophysiology to clinical practice

Sebastiani, G., & Pantopoulos, K. (2011) · Metallomics · doi:10.1039/c1mt00082a · Cited by 57 · see citing works

Comparative Genomics of Trace Element Dependence in Biology

Zhang, Y., & Gladyshev, V. N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.172833 · Cited by 56 · see citing works

Promotion of airway anastomotic microvascular regeneration and alleviation of airway ischemia by deferoxamine nanoparticles

Jiang, X., Malkovskiy, A. V., Tian, W., Sung, Y. K., Sun, W., Hsu, J. L., Manickam, S., Wagh, D. A., Joubert, L., Semenza, G. L., et al. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.09.092 · Cited by 55 · see citing works

Quantitative high-field imaging of sub-cortical gray matter in multiple sclerosis

Lebel, R. M., Eissa, A., Seres, P., Blevins, G., & Wilman, A. H. (2011) · Multiple Sclerosis Journal · doi:10.1177/1352458511428464 · Cited by 55 · see citing works

Combination treatment of angiotensin II type I receptor blocker and new oral iron chelator attenuates progression of nonalcoholic steatohepatitis in rats

Kaji, K., Yoshiji, H., Kitade, M., Ikenaka, Y., Noguchi, R., Shirai, Y., Aihara, Y., Namisaki, T., Yoshii, J., Yanase, K., et al. (2011) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00365.2010 · Cited by 55 · see citing works

Microalgal food supplements from the perspective of Polish consumers: patterns of use, adverse events, and beneficial effects

Rzymski, P., & Jaśkiewicz, M. (2017) · Journal of Applied Phycology · doi:10.1007/s10811-017-1079-5 · Cited by 55 · see citing works

Fiber evanescent wave spectroscopy using the mid-infrared provides useful fingerprints for metabolic profiling in humans

Anne, M.-L., Lan, C. L., Monbet, V., Boussard‐Plédel, C., Ropert, M., Sire, O., Pouchard, M., Jard, C., Lucas, J., Adam, J., et al. (2009) · Journal of Biomedical Optics · doi:10.1117/1.3253319 · Cited by 54 · see citing works

The Mycobacterium tuberculosis transcriptional landscape under genotoxic stress

Namouchi, A., Gómez-Muñoz, M., Frye, S. A., Moen, L. V., Rognes, T., Tønjum, T., & Balasingham, S. V. (2016) · BMC Genomics · doi:10.1186/s12864-016-3132-1 · Cited by 52 · see citing works

Iron in intracellular infection: to provide or to deprive?

Silva-Gomes, S., Vale-Costa, S., Appelberg, R., & Gomes, M. S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00096 · Cited by 51 · see citing works

Aerobactin-Mediated Iron Acquisition Enhances Biofilm Formation, Oxidative Stress Resistance, and Virulence of Yersinia pseudotuberculosis

Li, C., Pan, D., Li, M., Wang, Y., Song, L., Yu, D., Zuo, Y., Wang, K., Liu, Y., Wei, Z., et al. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.699913 · Cited by 54 · see citing works

Iron overload causes oxidative stress and impaired insulin signaling in AML-12 hepatocytes

Messner, D. J., Rhieu, B., & Kowdley, K. (2013) · Digestive Diseases and Sciences · doi:10.1007/s10620-013-2648-3 · Cited by 53 · see citing works

Hepcidin: another culprit for complications in patients with chronic kidney disease?

Nakanishi, T., Hasuike, Y., Otaki, Y., Kida, A., Nonoguchi, H., & Kuragano, T. (2011) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfr410 · Cited by 53 · see citing works

Ferroptosis increases obesity: Crosstalk between adipocytes and the neuroimmune system

Zhang, S., Sun, Z., Jiang, X. Y., Lu, Z., Ding, L., Li, C., Tian, X., & Wang, Q. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1049936 · Cited by 52 · see citing works

Oral iron supplementation leads to oxidative imbalance in anemic women: A prospective study

Tiwari, A. K. M., Mahdi, A. A., Chandyan, S., Zahra, F. T., Godbole, M., Jaiswar, S. P., Srivastava, V. K., & Negi, M. P. S. (2010) · Clinical Nutrition · doi:10.1016/j.clnu.2010.08.001 · Cited by 52 · see citing works

Differences in activation of mouse hepcidin by dietary iron and parenterally administered iron dextran: compartmentalization is critical for iron sensing

Daba, A., Gkouvatsos, K., Sebastiani, G., & Pantopoulos, K. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0937-5 · Cited by 52 · see citing works

Iron-rich Kupffer cells exhibit phenotypic changes during the development of liver fibrosis in NASH

Kanamori, Y., Tanaka, M., Itoh, M., Ochi, K., Ito, A., Hidaka, I., Sakaida, I., Ogawa, Y., & Suganami, T. (2021) · iScience · doi:10.1016/j.isci.2020.102032 · Cited by 45 · see citing works

Modulatory effects of lipoic acid and selenium against cadmium‐induced biochemical alterations in testicular steroidogenesis

El‐Maraghy, S. A., & Nassar, N. N. (2010) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.20354 · Cited by 51 · see citing works

F-box and leucine-rich repeat protein 5 (FBXL5): Sensing intracellular iron and oxygen

Ruiz, J. C., & Bruick, R. K. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.01.015 · Cited by 51 · see citing works

Iron and vascular calcification. Is there a link?

Neven, E., Schutter, T. M. D., Behets, G. J. S., Gupta, A., & D’Haese, P. C. (2011) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfq858 · Cited by 50 · see citing works

The acute toxicity of iron and copper: Biomolecule oxidation and oxidative damage in rat liver

Boveris, A., Musacco-Sebio, R., Ferrarotti, N., Saporito-Magriñá, C., Torti, H., Massot, F., & Repetto, M. G. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.07.004 · Cited by 48 · see citing works

Iron overload exacerbates age-associated cardiac hypertrophy in a mouse model of hemochromatosis

Sukumaran, A., Chang, J., Han, M., Mintri, S., Khaw, B., & Kim, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-05810-2 · Cited by 48 · see citing works

Chronic expression of H-ferritin in dopaminergic midbrain neurons results in an age-related expansion of the labile iron pool and subsequent neurodegeneration: implications for Parkinson's disease

Kaur, D., Rajagopalan, S., & Andersen, J. K. (2009) · Brain Research · doi:10.1016/j.brainres.2009.08.043 · Cited by 48 · see citing works

HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis

Shan, Y., & Cortopassi, G. A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr582 · Cited by 47 · see citing works

Hemerythrin-like Domain within F-box and Leucine-rich Repeat Protein 5 (FBXL5) Communicates Cellular Iron and Oxygen Availability by Distinct Mechanisms

Chollangi, S., Thompson, J. W., Ruiz, J. C., Gardner, K. H., & Bruick, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.360404 · Cited by 46 · see citing works

Lipophilic Caffeic Acid Derivatives Protect Cells against H2O2-Induced DNA Damage by Chelating Intracellular Labile Iron

Kitsati, N., Fokas, D., Ouzouni, M., Mantzaris, M. D., Barbouti, A., & Galaris, D. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf301237y · Cited by 46 · see citing works

Plasma levels of advanced glycation end products are associated with haemolysis‐related organ complications in sickle cell patients

Nur, E., Brandjes, D. P. M., Schnog, J. B., Otten, H.-M. M. B., Fijnvandraat, K., Schalkwijk, C. G., Biemond, B. J., & the CURAMA Study Group (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08320.x · Cited by 45 · see citing works

Coaction of hepatic thioredoxin and glutathione systems in iron overload‐induced oxidative stress

Aydın, F. S., Hukkamlı, B., & Budak, H. (2021) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22704 · Cited by 45 · see citing works

Integration of epidemiological and blood biomarker analysis links haem iron intake to increased type 2 diabetes risk

Wang, F., Glenn, A. J., Tessier, A., Mei, Z., Haslam, D. E., Guasch‐Ferré, M., Tobias, D. K., Eliassen, A. H., Manson, J. E., Clish, C. B., et al. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01109-5 · Cited by 47 · see citing works

Oxidative stress and aging: the potential role of iron

Galaris, D., Mantzaris, M. D., & Amorgianiotis, C. (2008) · HORMONES · doi:10.1007/bf03401502 · Cited by 44 · see citing works

Lipophilic ester and amide derivatives of rosmarinic acid protect cells against H2O2-induced DNA damage and apoptosis: The potential role of intracellular accumulation and labile iron chelation

Gerogianni, P. S., Chatziathanasiadou, Μ. V., Diamantis, D. A., Tzakos, A. G., & Galaris, D. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.014 · Cited by 44 · see citing works

IdeR, a DtxR Family Iron Response Regulator, Controls Iron Homeostasis, Morphological Differentiation, Secondary Metabolism, and the Oxidative Stress Response in Streptomyces avermitilis

Cheng, Y., Yang, R., Lyu, M., Wang, S., Liu, X., Wen, Y., Song, Y., Li, J., & Chen, Z. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.01503-18 · Cited by 44 · see citing works

Iron increases liver injury through oxidative/nitrative stress in diabetic rats: Involvement of nitrotyrosination of glucokinase

Li, X., Li, H., Lu, N., Feng, Y., Huang, Y., & Gao, Z. (2012) · Biochimie · doi:10.1016/j.biochi.2012.07.019 · Cited by 42 · see citing works

Effect of a Prolonged Dietary Iron Intake on the Gene Expression and Activity of the Testicular Antioxidant Defense System in Rats

Koçpınar, E. F., Baltacı, N. G., Ceylan, H., Kalın, Ş. N., Erdoğan, O., & Budak, H. (2019) · Biological Trace Element Research · doi:10.1007/s12011-019-01817-0 · Cited by 41 · see citing works

The role of Fenton reaction in ROS-induced toxicity underlying atherosclerosis – modeled and analyzed using a Petri net-based approach

Formanowicz, D., Radom, M., Rybarczyk, A., & Formanowicz, P. (2018) · Biosystems · doi:10.1016/j.biosystems.2018.01.002 · Cited by 41 · see citing works

Cardioprotective strategies against doxorubicin-induced cardiotoxicity: A review from standard therapies to emerging mitochondrial transplantation

Ito‐Hagiwara, K., Hagiwara, J., Endo, Y., Becker, L. B., & Hayashida, K. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118315 · Cited by 40 · see citing works

Time-dependent changes in protein expression in rainbow trout muscle following hypoxia

Wulff, T., Jokumsen, A., Højrup, P., & Jessen, F. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.02.010 · Cited by 40 · see citing works

Dual Role of ROS as Signal and Stress Agents: Iron Tips the Balance in favor of Toxic Effects

Gammella, E., Recalcati, S., & Cairo, G. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8629024 · Cited by 106 · see citing works

Iron homeostasis and oxidative stress: An intimate relationship

Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 922 · see citing works

Role of Iron in Metabolic Disorders via ROS Influence on Inflammation

Chaudhary, P., Madan, A., Saxena, D., Kriti, K., Singh, S., Bhise, M. R., Mondal, M., Chakraborty, A. J., & Debnath, B. (2026) · Springer eBooks · doi:10.1007/978-3-032-11752-6_18

Oxidative Stress and the Homeodynamics of Iron Metabolism

Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247 · see citing works

Iron Metabolism and Oxidative Stress

Zarjou, A., Balla, J., Balla, G., & Agarwal, A. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-857-7_11 · Cited by 7 · see citing works